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sf9 suspension insect cells  (Expression Systems Inc)


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    Expression Systems Inc sf9 suspension insect cells
    Sf9 Suspension Insect Cells, supplied by Expression Systems Inc, used in various techniques. Bioz Stars score: 99/100, based on 4776 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/sf9+suspension+insect+cells/Sf9+Cells/us12385914-360-17-21
    Average 99 stars, based on 4776 article reviews
    sf9 suspension insect cells - by Bioz Stars, 2026-09
    99/100 stars

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    Expressing:

    Article Title: Interactions with and within mammalian cryptochromes regulate circadian rhythms
    Article Snippet: .. 2.5 Materials and Methods 2.5.1 Protein expression and purification Using the baculovirus expression system (Invitrogen), the following constructs were expressed in Sf9 suspension insect cells (Expression Systems): His-tagged mouse CRY1 PHR domain (residues 1–491), CRY2 PHR domain (residues 1–512), CRY2 7M PHR domain (residues 1–512 with the following mutations: A61G, S64N, S394E, V396M, R397K, D400E, F408W), CRY2 2M PHR domain (residues 1–512 with the following mutations: A61G, S64N) CLOCK:BMAL1 bHLH-PAS domains (CLOCK residues 26–395, BMAL1 residues 62–441) or GST-tagged BMAL1 PAS-AB domains (residues 136–441). ..

    Article Title: CRY1-clock-BMAL1 complex-disrupting agents and methods of identifying and using same
    Article Snippet: .. Protein Expression and Purification Using the baculovirus expression system (Invitrogen), His6-tagged mouse CRY1 PHR was expressed in Sf9 suspension insect cells (Expression Systems). ..

    Purification:

    Article Title: Interactions with and within mammalian cryptochromes regulate circadian rhythms
    Article Snippet: .. 2.5 Materials and Methods 2.5.1 Protein expression and purification Using the baculovirus expression system (Invitrogen), the following constructs were expressed in Sf9 suspension insect cells (Expression Systems): His-tagged mouse CRY1 PHR domain (residues 1–491), CRY2 PHR domain (residues 1–512), CRY2 7M PHR domain (residues 1–512 with the following mutations: A61G, S64N, S394E, V396M, R397K, D400E, F408W), CRY2 2M PHR domain (residues 1–512 with the following mutations: A61G, S64N) CLOCK:BMAL1 bHLH-PAS domains (CLOCK residues 26–395, BMAL1 residues 62–441) or GST-tagged BMAL1 PAS-AB domains (residues 136–441). ..

    Article Title: CRY1-clock-BMAL1 complex-disrupting agents and methods of identifying and using same
    Article Snippet: .. Protein Expression and Purification Using the baculovirus expression system (Invitrogen), His6-tagged mouse CRY1 PHR was expressed in Sf9 suspension insect cells (Expression Systems). ..

    Article Title: CRY2 missense mutations suppress P53 and enhance cell growth
    Article Snippet: GenePattern ( https://www.genepattern.org/use-genepattern ), GSEA ( 57 ), and differential expression analysis (using R [ https://www.r-project.org/ ]) were used to analyze the RNA sequencing (RNA-seq) data for differentially expressed genes and to find suppressed or enriched gene sets across samples. . BLI. .. Polyhistidine (His)-tagged mouse CRY2 D325H PHR domain was expressed in Sf9-suspension insect cells (Expression Systems) and was purified as described in detail in SI Appendix , Materials and Methods . ..

    Construct:

    Article Title: Interactions with and within mammalian cryptochromes regulate circadian rhythms
    Article Snippet: .. 2.5 Materials and Methods 2.5.1 Protein expression and purification Using the baculovirus expression system (Invitrogen), the following constructs were expressed in Sf9 suspension insect cells (Expression Systems): His-tagged mouse CRY1 PHR domain (residues 1–491), CRY2 PHR domain (residues 1–512), CRY2 7M PHR domain (residues 1–512 with the following mutations: A61G, S64N, S394E, V396M, R397K, D400E, F408W), CRY2 2M PHR domain (residues 1–512 with the following mutations: A61G, S64N) CLOCK:BMAL1 bHLH-PAS domains (CLOCK residues 26–395, BMAL1 residues 62–441) or GST-tagged BMAL1 PAS-AB domains (residues 136–441). ..

    Article Title: Interactions with and within mammalian cryptochromes regulate circadian rhythms
    Article Snippet: .. BMAL1 PAS-AB (mouse BMAL1 residues 136-441) and all CRY constructs containing the PHR domain (mouse CRY1 PHR, residues 1-491; mouse CRY2 PHR, residues 1-512) were expressed in Sf9 suspension insect cells (Expression systems) using the baculovirus expression system. ..

    Suspension:

    Article Title: Interactions with and within mammalian cryptochromes regulate circadian rhythms
    Article Snippet: .. 2.5 Materials and Methods 2.5.1 Protein expression and purification Using the baculovirus expression system (Invitrogen), the following constructs were expressed in Sf9 suspension insect cells (Expression Systems): His-tagged mouse CRY1 PHR domain (residues 1–491), CRY2 PHR domain (residues 1–512), CRY2 7M PHR domain (residues 1–512 with the following mutations: A61G, S64N, S394E, V396M, R397K, D400E, F408W), CRY2 2M PHR domain (residues 1–512 with the following mutations: A61G, S64N) CLOCK:BMAL1 bHLH-PAS domains (CLOCK residues 26–395, BMAL1 residues 62–441) or GST-tagged BMAL1 PAS-AB domains (residues 136–441). ..

    Article Title: Quantification of protein abundance and interaction defines a mechanism for operation of the circadian clock
    Article Snippet: Cleaved proteins were collected from the flow-through; GST-BirA was further purified using size exclusion chromatography (SEC) on a Superdex75 column (GE Healthcare) in 50 mM Tris, pH 8.0, 300 mM NaCl, 1 mM dithiothreitol (DTT), and 5% (vol/vol) glycerol, while CLOCK PAS-AB was further purified using SEC in 20 mM HEPES pH 7.5, 125 mM NaCl, 5% (vol/vol) glycerol, and 2 mM Tris(2-carboxyethyl)phosphine (TCEP). .. BMAL1 PAS-AB (mouse BMAL1 residues 136–441) was expressed in Sf9 suspension insect cells (Expression systems) as a GST-tagged protein using the baculovirus expression system. ..

    Article Title: CRY1-clock-BMAL1 complex-disrupting agents and methods of identifying and using same
    Article Snippet: .. Protein Expression and Purification Using the baculovirus expression system (Invitrogen), His6-tagged mouse CRY1 PHR was expressed in Sf9 suspension insect cells (Expression Systems). ..

    Article Title: CRY2 missense mutations suppress P53 and enhance cell growth
    Article Snippet: GenePattern ( https://www.genepattern.org/use-genepattern ), Gene Set Enrichment Analysis (GSEA) , and differential expression analysis (DESeq2) (using R ( https://www.r-project.org/ )) were used to analyze the RNA-seq data for differentially expressed genes and to find suppressed or enriched gene sets across samples. .. His-tagged mouse CRY2 D325H PHR domain (residues 1-512) was expressed in Sf9 suspension insect cells (Expression Systems, Davis, CA) infected with a P3 baculovirus at 1.2 × 10 6 cells per milliliter and grown for 72 hours at 27°C with gentle shaking. .. Cells were centrifuged at 4°C for 4000 × rpm for 15 minutes and resuspended in 50 mM Tris buffer pH 7.5, 300 mM NaCl, 20 mM imidazole, 10% (vol/vol) glycerol, 0.1% (vol/vol) Triton X-100, 5 mM β-mercaptoethanol and EDTA-free protease inhibitors (Pierce, Waltham, Massachusetts,).

    Article Title: Interactions with and within mammalian cryptochromes regulate circadian rhythms
    Article Snippet: .. BMAL1 PAS-AB (mouse BMAL1 residues 136-441) and all CRY constructs containing the PHR domain (mouse CRY1 PHR, residues 1-491; mouse CRY2 PHR, residues 1-512) were expressed in Sf9 suspension insect cells (Expression systems) using the baculovirus expression system. ..

    Article Title: CHRONO participates in multi-modal repression of circadian transcriptional complexes
    Article Snippet: .. Mouse CRY1 PHR domain (residues 1-491) was expressed in Sf9 suspension insect cells (Expression Systems) as previously described ( ). .. Cells were centrifuged at 4 °C at 3,200 × g , resuspended in 50 mM Tris, pH 7.5, 300 mM NaCl, 5% (vol/vol) glycerol, and 5 mM BME and lysed in low concentrations of detergent (0.01% Triton X-100), EDTA-free protease inhibitor tablets (Roche), and 1 mM phenylmethylsulfonyl fluoride using a high-pressure extruder (Avestin) followed by brief sonication on ice.

    Infection:

    Article Title: CRY2 missense mutations suppress P53 and enhance cell growth
    Article Snippet: GenePattern ( https://www.genepattern.org/use-genepattern ), Gene Set Enrichment Analysis (GSEA) , and differential expression analysis (DESeq2) (using R ( https://www.r-project.org/ )) were used to analyze the RNA-seq data for differentially expressed genes and to find suppressed or enriched gene sets across samples. .. His-tagged mouse CRY2 D325H PHR domain (residues 1-512) was expressed in Sf9 suspension insect cells (Expression Systems, Davis, CA) infected with a P3 baculovirus at 1.2 × 10 6 cells per milliliter and grown for 72 hours at 27°C with gentle shaking. .. Cells were centrifuged at 4°C for 4000 × rpm for 15 minutes and resuspended in 50 mM Tris buffer pH 7.5, 300 mM NaCl, 20 mM imidazole, 10% (vol/vol) glycerol, 0.1% (vol/vol) Triton X-100, 5 mM β-mercaptoethanol and EDTA-free protease inhibitors (Pierce, Waltham, Massachusetts,).

    Gentle:

    Article Title: CRY2 missense mutations suppress P53 and enhance cell growth
    Article Snippet: GenePattern ( https://www.genepattern.org/use-genepattern ), Gene Set Enrichment Analysis (GSEA) , and differential expression analysis (DESeq2) (using R ( https://www.r-project.org/ )) were used to analyze the RNA-seq data for differentially expressed genes and to find suppressed or enriched gene sets across samples. .. His-tagged mouse CRY2 D325H PHR domain (residues 1-512) was expressed in Sf9 suspension insect cells (Expression Systems, Davis, CA) infected with a P3 baculovirus at 1.2 × 10 6 cells per milliliter and grown for 72 hours at 27°C with gentle shaking. .. Cells were centrifuged at 4°C for 4000 × rpm for 15 minutes and resuspended in 50 mM Tris buffer pH 7.5, 300 mM NaCl, 20 mM imidazole, 10% (vol/vol) glycerol, 0.1% (vol/vol) Triton X-100, 5 mM β-mercaptoethanol and EDTA-free protease inhibitors (Pierce, Waltham, Massachusetts,).



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    BL2*21:01 linked to the MDV pp38 peptide was <t>expressed</t> <t>in</t> <t>insect</t> cells and purified, and has a similar thermostability as other chicken class II molecules bound to MDV peptides. A. Cartoon showing full-length construct, with scissors indicating the potential cleavage sites of endoproteinase Glu-C (Endoproteinase V8). B. UV traces of FPLC size-exclusion chromatography (SEC) using Superdex S200 column, before (blue) and after (black) being subjected to Endoproteinase V8 cleavage at 37°C overnight to remove C-terminal tags and dimerization domains. C. SDS-PAGE followed by Coomassie blue staining after initial nickel column purification (Input) and SEC fractions comprising Peak1 (blue trace of profile in A). Standard protein markers with indicated molecular masses; blue arrows indicate position of α- and β-chains. D. SDS-PAGE followed by Coomassie blue staining of endoproteinase V8 on its own, Peak1 (blue trace of profile in A), and SEC fractions from Single Peak (black trace). Standard makers and blue arrows is in C, black arrows indicate the position of the endoproteinase V8 cleaved α- and β-chains. E. Thermal denaturation curves for BL2*02:01 molecules expressed with MDV peptides from glycoprotein H (gH, with melting temperature 69°C), glycoprotein E (gE, 75°C), and unique long gene 43 tegument protein (UL43, 78°C), compared to BL2*021:01 molecule expressed with MDV pp38 peptide.
    Sf9 Insect Suspension Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    sf9 suspension insect cells  (Expression Systems Inc)
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    Expression Systems Inc sf9 suspension insect cells
    BL2*21:01 linked to the MDV pp38 peptide was <t>expressed</t> <t>in</t> <t>insect</t> cells and purified, and has a similar thermostability as other chicken class II molecules bound to MDV peptides. A. Cartoon showing full-length construct, with scissors indicating the potential cleavage sites of endoproteinase Glu-C (Endoproteinase V8). B. UV traces of FPLC size-exclusion chromatography (SEC) using Superdex S200 column, before (blue) and after (black) being subjected to Endoproteinase V8 cleavage at 37°C overnight to remove C-terminal tags and dimerization domains. C. SDS-PAGE followed by Coomassie blue staining after initial nickel column purification (Input) and SEC fractions comprising Peak1 (blue trace of profile in A). Standard protein markers with indicated molecular masses; blue arrows indicate position of α- and β-chains. D. SDS-PAGE followed by Coomassie blue staining of endoproteinase V8 on its own, Peak1 (blue trace of profile in A), and SEC fractions from Single Peak (black trace). Standard makers and blue arrows is in C, black arrows indicate the position of the endoproteinase V8 cleaved α- and β-chains. E. Thermal denaturation curves for BL2*02:01 molecules expressed with MDV peptides from glycoprotein H (gH, with melting temperature 69°C), glycoprotein E (gE, 75°C), and unique long gene 43 tegument protein (UL43, 78°C), compared to BL2*021:01 molecule expressed with MDV pp38 peptide.
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    suspension sf9 insect cells  (Expression Systems Inc)
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    Image Search Results


    BL2*21:01 linked to the MDV pp38 peptide was expressed in insect cells and purified, and has a similar thermostability as other chicken class II molecules bound to MDV peptides. A. Cartoon showing full-length construct, with scissors indicating the potential cleavage sites of endoproteinase Glu-C (Endoproteinase V8). B. UV traces of FPLC size-exclusion chromatography (SEC) using Superdex S200 column, before (blue) and after (black) being subjected to Endoproteinase V8 cleavage at 37°C overnight to remove C-terminal tags and dimerization domains. C. SDS-PAGE followed by Coomassie blue staining after initial nickel column purification (Input) and SEC fractions comprising Peak1 (blue trace of profile in A). Standard protein markers with indicated molecular masses; blue arrows indicate position of α- and β-chains. D. SDS-PAGE followed by Coomassie blue staining of endoproteinase V8 on its own, Peak1 (blue trace of profile in A), and SEC fractions from Single Peak (black trace). Standard makers and blue arrows is in C, black arrows indicate the position of the endoproteinase V8 cleaved α- and β-chains. E. Thermal denaturation curves for BL2*02:01 molecules expressed with MDV peptides from glycoprotein H (gH, with melting temperature 69°C), glycoprotein E (gE, 75°C), and unique long gene 43 tegument protein (UL43, 78°C), compared to BL2*021:01 molecule expressed with MDV pp38 peptide.

    Journal: bioRxiv

    Article Title: A major histocompatibility complex (MHC) class II molecule that binds the same viral pathogen peptide with both nonamer and decamer core sequences for presentation to T cells

    doi: 10.1101/2025.10.27.684722

    Figure Lengend Snippet: BL2*21:01 linked to the MDV pp38 peptide was expressed in insect cells and purified, and has a similar thermostability as other chicken class II molecules bound to MDV peptides. A. Cartoon showing full-length construct, with scissors indicating the potential cleavage sites of endoproteinase Glu-C (Endoproteinase V8). B. UV traces of FPLC size-exclusion chromatography (SEC) using Superdex S200 column, before (blue) and after (black) being subjected to Endoproteinase V8 cleavage at 37°C overnight to remove C-terminal tags and dimerization domains. C. SDS-PAGE followed by Coomassie blue staining after initial nickel column purification (Input) and SEC fractions comprising Peak1 (blue trace of profile in A). Standard protein markers with indicated molecular masses; blue arrows indicate position of α- and β-chains. D. SDS-PAGE followed by Coomassie blue staining of endoproteinase V8 on its own, Peak1 (blue trace of profile in A), and SEC fractions from Single Peak (black trace). Standard makers and blue arrows is in C, black arrows indicate the position of the endoproteinase V8 cleaved α- and β-chains. E. Thermal denaturation curves for BL2*02:01 molecules expressed with MDV peptides from glycoprotein H (gH, with melting temperature 69°C), glycoprotein E (gE, 75°C), and unique long gene 43 tegument protein (UL43, 78°C), compared to BL2*021:01 molecule expressed with MDV pp38 peptide.

    Article Snippet: Sf9 insect suspension cells ( Spodoptera frugiperda female ovarian cell line, ATCC CRL-1711) were used for production of baculovirus, and High Five insect suspension cells ( Trichoplusia ni female ovarian cell line, GIBCO B85502) were used for protein production, both grown in Insect-XPRESS Protein-free Insect Cell Medium (Lonza, BE12-730Q) supplemented with L-glutamine (to 1%), 50 U/ml penicillin, and 50 μg/ml streptomycin at 27°C with shaking at 135 rpm.

    Techniques: Purification, Construct, Size-exclusion Chromatography, SDS Page, Staining, Nickel Column